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2.7.4.2: phosphomevalonate kinase

This is an abbreviated version!
For detailed information about phosphomevalonate kinase, go to the full flat file.

Word Map on EC 2.7.4.2

Reaction

ATP
+
(R)-5-phosphomevalonate
=
ADP
 +
(R)-5-diphosphomevalonate

Synonyms

5-phosphomevalonate kinase, ATP:5-phosphomevalonate phosphotransferase, CcPMK, ERG8, GbPMK, kinase, phosphomevalonate (phosphorylating), mevalonate phosphate kinase, mevalonate-5-phosphate kinase, mevalonic acid phosphate kinase, More, phosphomevalonate kinase, phosphomevalonic kinase, PMK, PMVAK, PMVK, SSO2988

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.2 phosphomevalonate kinase

Engineering

Engineering on EC 2.7.4.2 - phosphomevalonate kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D23N
site-directed mutagenesis, the mutant shows highly reduced activity in both forward and reverse reactions compared to the wild-type enzyme
K17M
site-directed mutagenesis, the mutant shows reduced activity in both forward and reverse reactions compared to the wild-type enzyme
K19M
site-directed mutagenesis, the mutant shows highly reduced activity in both forward and reverse reactions compared to the wild-type enzyme
K22M
site-directed mutagenesis, the mutant shows a 10000fold reduced activity in both forward and reverse reactions compared to the wild-type enzyme, almost inactive mutant
K69M
mutant exhibits diminished Vmax values in both reaction directions with only slight Km perturbations
R110M
R111M
R130M
R138M
R141M
R18Q
site-directed mutagenesis, the mutant shows highly reduced activity in both forward and reverse reactions compared to the wild-type enzyme
A293T
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
K101M
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
K101R
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
K9M
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
K9R
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
additional information
analysis of the genetic basis of disseminated superficial porokeratosis (DSP) in two five-generation Chinese families with members diagnosed with DSP, whole-exome sequencing and genotyping. Identification of a nonsense variation c.412C > T (p.Arg138*) in the phosphomevalonate kinase gene (PMVK), which encodes a cytoplasmic enzyme catalyzing the conversion of mevalonate 5-phosphate to mevalonate 5-diphosphate in the mevalonate pathway. This genetic variant is involved in the development of DSP in both families. Using HaCaT cells as models, it is revealed that this variant disturbs subcellular localization, expression, and solubility of PMVK, apparent apoptosis in and under the cornoid lamella of PMVK-deficient lesional tissues is observed, with incomplete differentiation of keratinocytes. The R138* mutant shows reduced expression and solubility. Phenotypes, overview